منابع مشابه
Functional characterization of SlscADH1, a fruit-ripening-associated short-chain alcohol dehydrogenase of tomato.
A tomato short-chain dehydrogenase-reductase (SlscADH1) is preferentially expressed in fruit with a maximum expression at the breaker stage while expression in roots, stems, leaves and flowers is very weak. It represents a potential candidate for the formation of aroma volatiles by interconverting alcohols and aldehydes. The SlscADH1 recombinant protein produced in Escherichia coli exhibited de...
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Drosophila alcohol dehydrogenasc (alcohol:NADf oxidorcduct.ase, EC 1.1.1.1) has attracted attention in several laboratories (l-3) recently. Genetic variants of this enzyme were found, and consequently it was possible to determine its structural locus on the genetic map. The specific activity of alcohol dehydrogenase varies greatly along the t.ime axis of devcloprnent of this organism, and it oc...
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We read with a great pleasure the article ‘Rare ADH variant constellations are specific for alcohol dependence’ by Zuo et al. (2012). We want to direct the speciality about the alcohol dehydrogenase (ADH) isoenzyme nomenclature to the readers of Alcohol and Alcoholism. Namely, the authors use an old isoenzyme nomenclature what can cause some confusion to not enough familiar readers. Electrophor...
متن کاملAlcohol Dehydrogenase with
Complexation of alcohol dehydrogenase (ADH) and trypsin with poly(diallyldimethyl-ammonium chloride) (PDADMAC) in dilute electrolyte solution was studied by turbidimetric titration, quasi-elastic light scattering (QELS), and electrophoretic light scattering (ELS). Both QELS and turbidimetric titration show that PDADMAC forms complexes with ADH and trypsin in 0.01M NaCl solution at pH ¢ 6.8 and ...
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The alcohol dehydrogenase from Methylobacterium organophilum, a facultative methane-oxidizing bacterium, has been purified to homogeneity as indicated by sodium dodecyl sulfate-gel electrophoresis. It has several properties in common with the alcohol dehydrogenases from other methylotrophic bacteria. The active enzyme is a dimeric protein, both subunits having molecular weights of about 62,000....
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ژورنال
عنوان ژورنال: FEBS Letters
سال: 1991
ISSN: 0014-5793
DOI: 10.1016/0014-5793(91)81379-m